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Related Experiment Video

Updated: Feb 14, 2026

High-throughput Antiviral Assays to Screen for Inhibitors of Zika Virus Replication

High-throughput Antiviral Assays to Screen for Inhibitors of Zika Virus Replication

Published on: October 30, 2021

Zika NS2B Protein: In Vitro Formation of Large Multimeric Networks.

Caleb Ponniah¹, Wahyu Surya¹, Jaume Torres¹

¹School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.

International Journal of Molecular Sciences

|February 13, 2026

Summary

Zika virus NS2B protein, unlike previously thought, forms complex multimers in membranes and detergents. This multimerization may be crucial for viral RNA replication and particle formation.

Keywords:

Flaviviridae family Zika virus flavivirus membrane proteins multimerization non-structural 2B protein

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Last Updated: Feb 14, 2026

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Rapid Generation of Amyloid from Native Proteins In vitro

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Published on: December 5, 2013

Area of Science:

Virology
Structural Biology
Biochemistry

Background:

Flaviviruses cause significant global health issues.
Non-structural (NS) proteins, such as NS2 and NS4, are crucial for flavivirus replication but their structures and oligomerization remain poorly understood due to hydrophobicity.
NS2B protein, a cofactor for NS3 protease, has known hydrophobic domains and a hydrophilic loop, but its oligomerization behavior is largely unexplored.

Purpose of the Study:

To investigate the oligomerization behavior of Zika virus NS2B protein (ZIKV NS2B).
To characterize ZIKV NS2B oligomerization in both detergent and lipid environments.
To explore the potential role of ZIKV NS2B multimerization in viral processes.

Main Methods:

Expression and characterization of ZIKV NS2B protein.
Oligomerization studies using crosslinking in liposomes.
Biophysical characterization via mass photometry and analytical ultracentrifugation in detergent.

Main Results:

ZIKV NS2B exhibits complex oligomerization, forming dimers to large multimers (>10) in both detergent and lipid environments.
AlphaFold predicted a monomeric model consistent with data, but could not confidently predict oligomeric states.
NS2B's tendency to oligomerize suggests a role in membrane destabilization and host ER reshaping during infection.

Conclusions:

ZIKV NS2B protein displays a complex oligomerization propensity, forming diverse multimeric states.
Multimerization of ZIKV NS2B may be essential for its function in viral RNA replication and particle formation.
Formation of biologically relevant ZIKV NS2B complexes likely requires interactions with other viral proteins (NS4A, NS4B) or host factors.